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KGP1_BOVIN
ID   KGP1_BOVIN              Reviewed;         671 AA.
AC   P00516; P21136;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=cGMP-dependent protein kinase 1;
DE            Short=cGK 1;
DE            Short=cGK1;
DE            EC=2.7.11.12;
DE   AltName: Full=cGMP-dependent protein kinase I;
DE            Short=cGKI;
GN   Name=PRKG1; Synonyms=PRKG1B, PRKGR1A, PRKGR1B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RX   PubMed=2546820; DOI=10.1016/0014-5793(89)81453-x;
RA   Wernet W., Flockerzi V., Hofmann F.;
RT   "The cDNA of the two isoforms of bovine cGMP-dependent protein kinase.";
RL   FEBS Lett. 251:191-196(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RC   TISSUE=Testis;
RX   PubMed=9099696; DOI=10.1074/jbc.272.16.10522;
RA   Ruth P., Pfeifer A., Kamm S., Klatt P., Dostmann W.R., Hofmann F.;
RT   "Identification of the amino acid sequences responsible for high affinity
RT   activation of cGMP kinase Ialpha.";
RL   J. Biol. Chem. 272:10522-10528(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-18; 90-375 AND 408-671, AND ACETYLATION AT SER-2.
RX   PubMed=6091741; DOI=10.1021/bi00313a030;
RA   Takio K., Wade R.D., Smith S.B., Krebs E.G., Walsh K.A., Titani K.;
RT   "Guanosine cyclic 3',5'-phosphate dependent protein kinase, a chimeric
RT   protein homologous with two separate protein families.";
RL   Biochemistry 23:4207-4218(1984).
RN   [4]
RP   PROTEIN SEQUENCE OF 14-105 (ISOFORM ALPHA), PHOSPHORYLATION AT THR-59, AND
RP   BLOCKAGE OF N-TERMINUS.
RC   TISSUE=Lung;
RX   PubMed=6304091; DOI=10.1016/s0021-9258(20)81923-1;
RA   Takio K., Smith S.B., Walsh K.A., Krebs E.G., Titani K.;
RT   "Amino acid sequence around a 'hinge' region and its 'autophosphorylation'
RT   site in bovine lung cGMP-dependent protein kinase.";
RL   J. Biol. Chem. 258:5531-5536(1983).
RN   [5]
RP   PROTEIN SEQUENCE OF 63-75 (ISOFORM BETA).
RC   TISSUE=Aorta;
RX   PubMed=2537306; DOI=10.1016/s0021-9258(19)84976-1;
RA   Wolfe L., Francis S.H., Corbin J.D.;
RT   "Properties of a cGMP-dependent monomeric protein kinase from bovine
RT   aorta.";
RL   J. Biol. Chem. 264:4157-4162(1989).
RN   [6]
RP   PROTEIN SEQUENCE OF 374-410, AND ATP-BINDING AT LYS-390.
RX   PubMed=6274862; DOI=10.1016/s0021-9258(19)68256-6;
RA   Hashimoto E., Takio K., Krebs E.G.;
RT   "Amino acid sequence at the ATP-binding site of cGMP-dependent protein
RT   kinase.";
RL   J. Biol. Chem. 257:727-733(1982).
RN   [7]
RP   PROTEIN SEQUENCE OF 79-82 (ISOFORM ALPHA), AND CHARACTERIZATION.
RX   PubMed=2822399; DOI=10.1111/j.1432-1033.1987.tb13395.x;
RA   Heil W.G., Landgraf W., Hofmann F.;
RT   "A catalytically active fragment of cGMP-dependent protein kinase.
RT   Occupation of its cGMP-binding sites does not affect its phosphotransferase
RT   activity.";
RL   Eur. J. Biochem. 168:117-121(1987).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=1325910; DOI=10.1111/j.1432-1033.1992.tb17209.x;
RA   Keilbach A., Ruth P., Hofmann F.;
RT   "Detection of cGMP dependent protein kinase isozymes by specific
RT   antibodies.";
RL   Eur. J. Biochem. 208:467-473(1992).
RN   [9]
RP   INTERACTION WITH IRAG1.
RX   PubMed=10724174; DOI=10.1038/35004606;
RA   Schlossmann J., Ammendola A., Ashman K., Zong X., Huber A., Neubauer G.,
RA   Wang G.-X., Allescher H.-D., Korth M., Wilm M., Hofmann F., Ruth P.;
RT   "Regulation of intracellular calcium by a signalling complex of IRAG, IP3
RT   receptor and cGMP kinase Ibeta.";
RL   Nature 404:197-201(2000).
RN   [10]
RP   INTERACTION WITH IRAG1.
RX   PubMed=11309393; DOI=10.1074/jbc.m101530200;
RA   Ammendola A., Geiselhoeringer A., Hofmann F., Schlossmann J.;
RT   "Molecular determinants of the interaction between the inositol 1,4,5-
RT   trisphosphate receptor-associated cGMP kinase substrate (IRAG) and cGMP
RT   kinase Ibeta.";
RL   J. Biol. Chem. 276:24153-24159(2001).
RN   [11]
RP   SUBUNIT.
RX   PubMed=12480535; DOI=10.1016/s0006-291x(02)02799-7;
RA   Koller A., Schlossmann J., Ashman K., Uttenweiler-Joseph S., Ruth P.,
RA   Hofmann F.;
RT   "Association of phospholamban with a cGMP kinase signaling complex.";
RL   Biochem. Biophys. Res. Commun. 300:155-160(2003).
RN   [12]
RP   INTERACTION WITH IRAG1.
RX   PubMed=16166082; DOI=10.1074/jbc.m507021200;
RA   Casteel D.E., Boss G.R., Pilz R.B.;
RT   "Identification of the interface between cGMP-dependent protein kinase
RT   Ibeta and its interaction partners TFII-I and IRAG reveals a common
RT   interaction motif.";
RL   J. Biol. Chem. 280:38211-38218(2005).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 79-356 IN COMPLEX WITH CAMP.
RX   PubMed=21893290; DOI=10.1016/j.str.2011.06.012;
RA   Osborne B.W., Wu J., McFarland C.J., Nickl C.K., Sankaran B., Casteel D.E.,
RA   Woods V.L. Jr., Kornev A.P., Taylor S.S., Dostmann W.R.;
RT   "Crystal structure of cGMP-dependent protein kinase reveals novel site of
RT   interchain communication.";
RL   Structure 19:1317-1327(2011).
CC   -!- FUNCTION: Serine/threonine protein kinase that acts as key mediator of
CC       the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates
CC       PRKG1, which phosphorylates serines and threonines on many cellular
CC       proteins. Numerous protein targets for PRKG1 phosphorylation are
CC       implicated in modulating cellular calcium, but the contribution of each
CC       of these targets may vary substantially among cell types. Proteins that
CC       are phosphorylated by PRKG1 regulate platelet activation and adhesion,
CC       smooth muscle contraction, cardiac function, gene expression, feedback
CC       of the NO-signaling pathway, and other processes involved in several
CC       aspects of the CNS like axon guidance, hippocampal and cerebellar
CC       learning, circadian rhythm and nociception. Smooth muscle relaxation is
CC       mediated through lowering of intracellular free calcium, by
CC       desensitization of contractile proteins to calcium, and by decrease in
CC       the contractile state of smooth muscle or in platelet activation.
CC       Regulates intracellular calcium levels via several pathways:
CC       phosphorylates IRAG1 and inhibits IP3-induced Ca(2+) release from
CC       intracellular stores, phosphorylation of KCNMA1 (BKCa) channels
CC       decreases intracellular Ca(2+) levels, which leads to increased opening
CC       of this channel. PRKG1 phosphorylates the canonical transient receptor
CC       potential channel (TRPC) family which inactivates the associated inward
CC       calcium current. Another mode of action of NO/cGMP/PKGI signaling
CC       involves PKGI-mediated inactivation of the Ras homolog gene family
CC       member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of
CC       this protein in myriad processes: regulation of RHOA translocation;
CC       decreasing contraction; controlling vesicle trafficking, reduction of
CC       myosin light chain phosphorylation resulting in vasorelaxation.
CC       Activation of PRKG1 by NO signaling alters also gene expression in a
CC       number of tissues. In smooth muscle cells, increased cGMP and PRKG1
CC       activity influence expression of smooth muscle-specific contractile
CC       proteins, levels of proteins in the NO/cGMP signaling pathway, down-
CC       regulation of the matrix proteins osteopontin and thrombospondin-1 to
CC       limit smooth muscle cell migration and phenotype. Regulates
CC       vasodilator-stimulated phosphoprotein (VASP) functions in platelets and
CC       smooth muscle (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.12;
CC   -!- ACTIVITY REGULATION: In the absence of cGMP, PRKG1 activity is
CC       suppressed by autoinhibitory contacts. {ECO:0000250}.
CC   -!- SUBUNIT: Isoform alpha: parallel homodimer or heterodimer and also
CC       heterotetramer. Interacts directly with PPP1R12A. Non-covalent dimer of
CC       dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This interaction targets
CC       PRKG1 to stress fibers to mediate smooth muscle cell relaxation and
CC       vasodilation in responses to rises in cGMP (By similarity). Isoform
CC       beta: antiparallel homodimer. Part of cGMP kinase signaling complex at
CC       least composed of ACTA2/alpha-actin, CNN1/calponin H1,
CC       PLN/phospholamban, PRKG1 and ITPR1. Interacts with IRAG1 (By
CC       similarity). Forms a stable complex with ITPR1, IRAG1, and isoform beta
CC       of PRKG1 (By similarity). Interacts with TRPC7 (via ankyrin repeat
CC       domain) (By similarity). Isoform alpha interacts with RGS2 (By
CC       similarity). Interacts with GTF2I (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P00516-1; P00516-1: PRKG1; NbExp=2; IntAct=EBI-10094497, EBI-10094497;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized with
CC       TRPC7 in the plasma membrane. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha; Synonyms=CGK1-alpha;
CC         IsoId=P00516-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=CGK1-beta;
CC         IsoId=P00516-2, P21136-1;
CC         Sequence=VSP_038713;
CC   -!- TISSUE SPECIFICITY: High concentrations are detected in various smooth
CC       muscle: lung, rumen, trachea, aorta, uterus and stomach. Isoform alpha
CC       is expressed predominantly in heart, cerebellum and lung, whereas the
CC       beta isoform is expressed in high concentrations in trachea, aorta,
CC       stomach and uterus. {ECO:0000269|PubMed:1325910}.
CC   -!- DOMAIN: Composed of an N-terminal leucine-zipper domain followed by an
CC       autoinhibitory domain, which mediate homodimer formation and inhibit
CC       kinase activity, respectively. Next, two cGMP-binding domains are
CC       followed by the catalytic domain at the C-terminus. Binding of cGMP to
CC       cGMP-binding domains results in a conformational change that activates
CC       kinase activity by removing the autoinhibitory domain from the
CC       catalytic cleft leaving the catalytic domain free to phosphorylate
CC       downstream substrates. Isoforms alpha and beta have identical cGMP-
CC       binding and catalytic domains but differ in their leucine zipper and
CC       autoinhibitory sequences and therefore differ in their dimerization
CC       substrates and kinase enzyme activity.
CC   -!- DOMAIN: Heterotetramerization is mediated by the interaction between a
CC       coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS,
CC       the myosin-binding subunit of the myosin phosphatase. {ECO:0000250}.
CC   -!- PTM: Autophosphorylation increases kinase activity. {ECO:0000250}.
CC   -!- PTM: 65 kDa monomer is produced by proteolytic cleavage.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cGMP subfamily. {ECO:0000305}.
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DR   EMBL; X16086; CAA34214.1; -; mRNA.
DR   EMBL; X54289; CAA38184.1; -; mRNA.
DR   EMBL; Y08961; CAA70155.1; -; mRNA.
DR   PIR; A00619; OKBOG.
DR   PIR; S05035; S05035.
DR   RefSeq; NP_776861.1; NM_174436.2. [P00516-1]
DR   RefSeq; XP_005225410.1; XM_005225353.2. [P00516-2]
DR   PDB; 3SHR; X-ray; 2.50 A; A/B=79-356.
DR   PDBsum; 3SHR; -.
DR   AlphaFoldDB; P00516; -.
DR   BMRB; P00516; -.
DR   SASBDB; P00516; -.
DR   SMR; P00516; -.
DR   BioGRID; 159293; 2.
DR   CORUM; P00516; -.
DR   DIP; DIP-59143N; -.
DR   IntAct; P00516; 3.
DR   STRING; 9913.ENSBTAP00000030518; -.
DR   BindingDB; P00516; -.
DR   ChEMBL; CHEMBL3183; -.
DR   iPTMnet; P00516; -.
DR   PRIDE; P00516; -.
DR   Ensembl; ENSBTAT00000024490; ENSBTAP00000024490; ENSBTAG00000018404. [P00516-1]
DR   Ensembl; ENSBTAT00000030539; ENSBTAP00000030518; ENSBTAG00000018404. [P00516-2]
DR   GeneID; 282004; -.
DR   KEGG; bta:282004; -.
DR   CTD; 5592; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018404; -.
DR   eggNOG; KOG0614; Eukaryota.
DR   GeneTree; ENSGT00940000154704; -.
DR   InParanoid; P00516; -.
DR   OMA; XTHYENG; -.
DR   BRENDA; 2.7.11.12; 908.
DR   Reactome; R-BTA-392517; Rap1 signalling.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000018404; Expressed in oocyte and 90 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004692; F:cGMP-dependent protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
DR   GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
DR   GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IEA:Ensembl.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd05572; STKc_cGK; 1.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR002374; cGMP_dep_kinase.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR031831; PKcGMP_CC.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR035014; STKc_cGK.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF16808; PKcGMP_CC; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR   PRINTS; PR00104; CGMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51206; SSF51206; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
KW   ATP-binding; cGMP; cGMP-binding; Coiled coil; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6091741"
FT   CHAIN           2..671
FT                   /note="cGMP-dependent protein kinase 1"
FT                   /id="PRO_0000086114"
FT   DOMAIN          360..619
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          620..671
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          2..102
FT                   /note="Required for dimerization"
FT   REGION          9..44
FT                   /note="Leucine-zipper"
FT   REGION          50..75
FT                   /note="Autoinhibitory domain"
FT                   /evidence="ECO:0000250"
FT   REGION          103..220
FT                   /note="cGMP-binding, high affinity"
FT                   /evidence="ECO:0000250"
FT   REGION          221..341
FT                   /note="cGMP-binding, low affinity"
FT                   /evidence="ECO:0000250"
FT   REGION          635..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2..59
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        651..671
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        484
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         167..170
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000269|PubMed:21893290,
FT                   ECO:0007744|PDB:3SHR"
FT   BINDING         167..170
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         177..178
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000269|PubMed:21893290,
FT                   ECO:0007744|PDB:3SHR"
FT   BINDING         177..178
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         282
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         291..294
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         301..302
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         336
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         366..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         390
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   SITE            78..79
FT                   /note="Cleavage"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:6091741"
FT   MOD_RES         59
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:6304091"
FT   MOD_RES         515
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C605"
FT   DISULFID        43
FT                   /note="Interchain"
FT   VAR_SEQ         1..89
FT                   /note="MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPST
FT                   HIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSER -> MGTLRDLQYALQEKIEEL
FT                   RQRDALIDELELELDQKDELIQKLQNELDKYRSVIRPATQQAQKQSASTLQGEPRTKRQ
FT                   AISAEPTAFDIQDLSHVTLPFYPKSPQ (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:2546820,
FT                   ECO:0000303|PubMed:9099696"
FT                   /id="VSP_038713"
FT   HELIX           88..99
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   TURN            102..106
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   HELIX           109..118
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          120..124
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          140..146
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          179..185
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          187..192
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   HELIX           194..216
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   HELIX           220..224
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   HELIX           227..233
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   TURN            234..236
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          238..242
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          257..270
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          273..275
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          279..285
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   HELIX           292..295
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          296..300
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   STRAND          302..317
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   HELIX           318..325
FT                   /evidence="ECO:0007829|PDB:3SHR"
FT   HELIX           333..354
FT                   /evidence="ECO:0007829|PDB:3SHR"
SQ   SEQUENCE   671 AA;  76419 MW;  9FE7A48422DA9CDF CRC64;
     MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP STHIGPRTTR
     AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD NDFMKNLELS QIQEIVDCMY
     PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV TKEGVKLCTM GPGKVFGELA ILYNCTRTAT
     VKTLVNVKLW AIDRQCFQTI MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET
     HYENGEYIIR QGARGDTFFI ISKGKVNVTR EDSPNEDPVF LRTLGKGDWF GEKALQGEDV
     RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA FFANLKLSDF
     NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT RQQEHIRSEK QIMQGAHSDF
     IVRLYRTFKD SKYLYMLMEA CLGGELWTIL RDRGSFEDST TRFYTACVVE AFAYLHSKGI
     IYRDLKPENL ILDHRGYAKL VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD
     YWSLGILMYE LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS
     ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD SFPEDNDEPP
     PDDNSGWDID F
 
 
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